[HTML][HTML] X-ray crystal structure of the liver X receptor β ligand binding domain: regulation by a histidine-tryptophan switch
S Williams, RK Bledsoe, JL Collins, S Boggs… - Journal of Biological …, 2003 - ASBMB
The x-ray crystal structures of the human liver X receptor β ligand binding domain
complexed to sterol and nonsterol agonists revealed a perpendicular histidinetryptophan
switch that holds the receptor in its active conformation. Hydrogen bonding interactions with
the ligand act to position the His-435 imidazole ring against the Trp-457 indole ring, allowing
an electrostatic interaction that holds the AF2 helix in the active position. The neutral
oxysterol 24 (S), 25-epoxycholesterol accepts a hydrogen bond from His-435 that positions …
complexed to sterol and nonsterol agonists revealed a perpendicular histidinetryptophan
switch that holds the receptor in its active conformation. Hydrogen bonding interactions with
the ligand act to position the His-435 imidazole ring against the Trp-457 indole ring, allowing
an electrostatic interaction that holds the AF2 helix in the active position. The neutral
oxysterol 24 (S), 25-epoxycholesterol accepts a hydrogen bond from His-435 that positions …